Abstract
Gelatine was crosslinked by means of an enzymatic treatment using tissue transglutaminase (tTGase) (Sigma) and microbial transglutaminase (mTGase) (Ajinomoto) which catalyses the formation of isopeptide bonds between the γ-carbonyl group of a glutamine residue and the ε-amino group of a lysine residue. The reaction is an interesting alternative to the traditional glutaraldehyde crosslinking, which has several drawbacks (e.g., in medical application) due to the toxicity of the chemical reagent. To further investigate the possibility to utilize the modified protein for tissue engineering application, TGase crosslinked gelatine was incorporated in a gellan matrix, a polysaccharide, to enhance the stability in aqueous media. Films obtained by casting were characterized by thermal analysis, chemical imaging, swelling behaviour and cell adhesion.
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Acknowledgements
Authors wish to thank the European Commission for financial support through STReP-project “High Performance Industrial Protein Matrices trough Bioprocessing”-HIPERMAX/NMP-3-CT-2003-505790. The authors also wish to thank G. Vozzi (IMCB-CNR Italy) for performing the cell adhesion test, R. Lantto (VTT Biotechnology, Finland) for providing the purified mTgase, E. Heine (DWI at RWTH Aachen, Germany) for determining the amino acid sequence of gelatin.
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Bertoni, F., Barbani, N., Giusti, P. et al. Transglutaminase Reactivity with Gelatine: Perspective Applications in Tissue Engineering. Biotechnol Lett 28, 697–702 (2006). https://doi.org/10.1007/s10529-006-9046-2
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DOI: https://doi.org/10.1007/s10529-006-9046-2